Protein crystals orientation in a magnetic field

Abstract

Nucleation and crystal growth of hen egg-white lysozyme, bovine pancreatic trypsin inhibitor and porcine pancreatic α-amylase were carried out in the presence of a magnetic field of 1.25 T produced by small permanent magnets. Crystals were oriented in the magnetic field, except when heterogeneous nucleation occurred. The orientation of protein crystals in the presence of a magnetic field can be attributed to the anisotropic diamagnetic susceptibility of proteins resulting from the large anisotropy of the α-helices due to the axial alignment of the peptide bonds.